title: Recognizing and remodeling the nucleosome.
abstract: The X-ray structure of the nucleosome core particle (NCP) has been a major milestone in the structural biology of chromatin. Since, our understanding how NCPs interact with multiple partners has been extending from single chromatin-binding domains recognizing post-translational modifications (PTMs) in histone tails towards the recognition of higher-order chromatin structure by multi-subunit chromatin remodeling complexes. The current review summarizes recent progress in the structural biology of nucleosome-recognition from chromatin-binding domains to multi-protein remodeling complexes.
authors.affiliation: European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, Heidelberg, Germany.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Glatt
authors.forename: Claudio
authors.initials: C
authors.lastname: Alfieri
authors.forename: Christoph W
authors.initials: CW
authors.lastname: Müller
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D042002:Chromatin Assembly and Disassembly; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D009698:Nucleoproteins / Q000737:chemistry / Q000378:metabolism; D009707:Nucleosomes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology
chemical_list: D004268:DNA-Binding Proteins; D008024:Ligands; D009698:Nucleoproteins; D009707:Nucleosomes; D000255:Adenosine Triphosphate; D004247:DNA